BMRB Entry 34358

Name: NMR solution structure of LSR2 binding domain.
Published: 2019-10-03

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PDB ID: 6qkp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34358
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR solution structure of LSR2 binding domain.

Deposition date:

2019-01-30

Original release date:

2019-10-03

Authors:

Barthe, P.; Cohen-Gonsaud, M.; Mukamolova, G.

Citation:

Citation: Alqaseer, Kawther; Turapov, Obolbek; Barthe, Philippe; Jagatia, Heena; De Visch, Angelique; Roumestand, Christian; Wegrzyn, Malgorzata; Bartek, Iona; Voskuil, Martin; O'Hare, Helen; Ajuh, Paul; Bottrill, Andrew; Witney, Adam; Cohen-Gonsaud, Martin; Waddell, Simon; Mukamolova, Galina. "Protein kinase B controls Mycobacterium tuberculosis growth via phosphorylation of the transcriptional regulator Lsr2 at threonine 112" Mol. Microbiol. 112, 1847-1862 (2019).
PubMed: 31562654

Assembly members:

Assembly members:
entity_1, polymer, 50 residues, 5396.921 Da.

Natural source:

Natural source: Common Name: Mycobacterium tuberculosis Taxonomy ID: 83332 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMSGSGRGRGAIDREQSAA IREWARRNGHNVSTRGRIPA DVIDAYHAAT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	53
1H chemical shifts	301

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 50 residues - 5396.921 Da.

1	GLY	HIS	MET	SER	GLY	SER	GLY	ARG	GLY	ARG
2	GLY	ALA	ILE	ASP	ARG	GLU	GLN	SER	ALA	ALA
3	ILE	ARG	GLU	TRP	ALA	ARG	ARG	ASN	GLY	HIS
4	ASN	VAL	SER	THR	ARG	GLY	ARG	ILE	PRO	ALA
5	ASP	VAL	ILE	ASP	ALA	TYR	HIS	ALA	ALA	THR

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D DQF-COSY	sample_2	isotropic	sample_conditions_1

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BMRB Entry 34358

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

1	GLY	HIS	MET	SER	GLY	SER	GLY	ARG	GLY	ARG
2	GLY	ALA	ILE	ASP	ARG	GLU	GLN	SER	ALA	ALA
3	ILE	ARG	GLU	TRP	ALA	ARG	ARG	ASN	GLY	HIS
4	ASN	VAL	SER	THR	ARG	GLY	ARG	ILE	PRO	ALA
5	ASP	VAL	ILE	ASP	ALA	TYR	HIS	ALA	ALA	THR

1	GLY	HIS	MET	SER	GLY	SER	GLY	ARG	GLY	ARG
2	GLY	ALA	ILE	ASP	ARG	GLU	GLN	SER	ALA	ALA
3	ILE	ARG	GLU	TRP	ALA	ARG	ARG	ASN	GLY	HIS
4	ASN	VAL	SER	THR	ARG	GLY	ARG	ILE	PRO	ALA
5	ASP	VAL	ILE	ASP	ALA	TYR	HIS	ALA	ALA	THR

1	GLY	HIS	MET	SER	GLY	SER	GLY	ARG	GLY	ARG
2	GLY	ALA	ILE	ASP	ARG	GLU	GLN	SER	ALA	ALA
3	ILE	ARG	GLU	TRP	ALA	ARG	ARG	ASN	GLY	HIS
4	ASN	VAL	SER	THR	ARG	GLY	ARG	ILE	PRO	ALA
5	ASP	VAL	ILE	ASP	ALA	TYR	HIS	ALA	ALA	THR